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The following term was not found in PubMed: Fmn-family
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Structure and function of the interacting domains of Spire and Fmn-family formins.
Vizcarra CL, Kreutz B, Rodal AA, Toms AV, Lu J, Zheng W, Quinlan ME, Eck MJ. Vizcarra CL, et al. Proc Natl Acad Sci U S A. 2011 Jul 19;108(29):11884-9. doi: 10.1073/pnas.1105703108. Epub 2011 Jul 5. Proc Natl Acad Sci U S A. 2011. PMID: 21730168 Free PMC article.
Their interaction requires the kinase noncatalytic C-lobe domain (KIND) domain of Spire and the C-terminal tail of the formin. ...The KIND domain is structurally similar to the C-lobe of protein kinases. The Fmn2 tail is coo …
Their interaction requires the kinase noncatalytic C-lobe domain (KIND) domain of Spire and the C-terminal tail …
Spire-1 contributes to the invadosome and its associated invasive properties.
Lagal V, Abrivard M, Gonzalez V, Perazzi A, Popli S, Verzeroli E, Tardieux I. Lagal V, et al. J Cell Sci. 2014 Jan 15;127(Pt 2):328-40. doi: 10.1242/jcs.130161. Epub 2013 Nov 8. J Cell Sci. 2014. PMID: 24213528
We investigated the contribution of the actin nucleator Spire-1 to invadosome structure and function, using Src-activated cells and cancer cells. ...Spire-1 interacts with the Rab3A GTPase, a key player in the regulation of exocytosis that is pr …
We investigated the contribution of the actin nucleator Spire-1 to invadosome structure and function, using Src-activat …
The WH2 Domain and Actin Nucleation: Necessary but Insufficient.
Dominguez R. Dominguez R. Trends Biochem Sci. 2016 Jun;41(6):478-490. doi: 10.1016/j.tibs.2016.03.004. Epub 2016 Apr 5. Trends Biochem Sci. 2016. PMID: 27068179 Free PMC article. Review.
PRDs serve as a platform for protein-protein interactions, often mediating the binding of profilin-actin. The WH2 domain is an abundant actin monomer-binding motif comprising 17 amino acids. ...Yet, it is argued here that the WH2 domain plays on …
PRDs serve as a platform for protein-protein interactions, often mediating the binding of profilin-actin. The WH2 do
Autoinhibition of the formin Cappuccino in the absence of canonical autoinhibitory domains.
Bor B, Vizcarra CL, Phillips ML, Quinlan ME. Bor B, et al. Mol Biol Cell. 2012 Oct;23(19):3801-13. doi: 10.1091/mbc.E12-04-0288. Epub 2012 Aug 8. Mol Biol Cell. 2012. PMID: 22875983 Free PMC article.
The Drosophila formin, Cappuccino (Capu), was believed to be an exception. Capu does not contain conserved autoinhibitory domains and can be regulated by a second protein, Spire. ...Hydrodynamic analysis indicates that Capu-NT is a dimer, similar to th …
The Drosophila formin, Cappuccino (Capu), was believed to be an exception. Capu does not contain conserved autoinhibitory domains
Actin filament nucleation and elongation factors--structure-function relationships.
Dominguez R. Dominguez R. Crit Rev Biochem Mol Biol. 2009 Nov-Dec;44(6):351-66. doi: 10.3109/10409230903277340. Crit Rev Biochem Mol Biol. 2009. PMID: 19874150 Free PMC article. Review.
Filament nucleators are generally unrelated, but with the exception of formins they all use the WASP-Homology 2 domain (WH2 or W), a small and versatile actin-binding motif, for interaction with actin. ...Formins are unique in that they use the form
Filament nucleators are generally unrelated, but with the exception of formins they all use the WASP-Homology 2 domain (WH2 or …
X-ray scattering study of actin polymerization nuclei assembled by tandem W domains.
Rebowski G, Boczkowska M, Hayes DB, Guo L, Irving TC, Dominguez R. Rebowski G, et al. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10785-90. doi: 10.1073/pnas.0801650105. Epub 2008 Jul 31. Proc Natl Acad Sci U S A. 2008. PMID: 18669664 Free PMC article.
The initiation of actin polymerization in cells requires actin filament nucleators. With the exception of formins, known filament nucleators use the Wiskott-Aldrich syndrome protein (WASP) homology 2 (WH2 or W) domain for interaction with actin. ...Unc …
The initiation of actin polymerization in cells requires actin filament nucleators. With the exception of formins, known filament nuc …